A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV

The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed…

• UD
  U.S. Department of Energy

  Awards: AC02-06CH11357, DE-AC02, 06CH11357, DE-AC02-06CH11357, DE-AC02-
• BA
  Bill and Melinda Gates Foundation

  Award: OPP1170236
• GM
  Guangzhou Medical University
• NN
  National Natural Science Foundation of China

  Awards: DE-AC02-06CH11357, N_HKU737/18
• IP
  Institut Pasteur
• NI
  National Institutes of Health

  Awards: AGM-12006, ACB-12002, K99 AI139445, DE-AC02-06CH11357
• OO
  Office of Science

  Awards: DE-AC02-06CH11357, DE-AC02, 06CH11357, AC02-06CH11357
• NC
  National Cancer Institute

  Awards: DE-AC02-06CH11357, ACB-12002, AGM-12006
• NI
  National Institute of General Medical Sciences

  Awards: DE-AC02-06CH11357, AGM-12006, ACB-12002
• NI
  National Institute of Allergy and Infectious Diseases

  Award: K99 AI139445
• AN
  Argonne National Laboratory

  Awards: DE-AC02, 06CH11357, AC02-06CH11357